DPO3B_MYCTO
ID DPO3B_MYCTO Reviewed; 402 AA.
AC P9WNU0; L0T229; O53602; Q50790;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 25-MAY-2022, entry version 37.
DE RecName: Full=Beta sliding clamp;
DE Short=Beta clamp;
DE Short=Sliding clamp;
DE AltName: Full=Beta-clamp processivity factor;
DE AltName: Full=DNA polymerase III beta sliding clamp subunit;
DE AltName: Full=DNA polymerase III subunit beta;
GN Name=dnaN; OrderedLocusNames=MT0002;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
RN [2] {ECO:0007744|PDB:4TR7}
RP X-RAY CRYSTALLOGRAPHY (2.29 ANGSTROMS), AND SUBUNIT.
RX PubMed=25170813; DOI=10.1021/jm500467a;
RA Wolff P., Amal I., Olieric V., Chaloin O., Gygli G., Ennifar E., Lorber B.,
RA Guichard G., Wagner J., Dejaegere A., Burnouf D.Y.;
RT "Differential modes of peptide binding onto replicative sliding clamps from
RT various bacterial origins.";
RL J. Med. Chem. 57:7565-7576(2014).
CC -!- FUNCTION: Confers DNA tethering and processivity to DNA polymerases and
CC other proteins. Acts as a clamp, forming a ring around DNA (a reaction
CC catalyzed by the clamp-loading complex) which diffuses in an ATP-
CC independent manner freely and bidirectionally along dsDNA. Initially
CC characterized for its ability to contact the catalytic subunit of DNA
CC polymerase III (Pol III), a complex, multichain enzyme responsible for
CC most of the replicative synthesis in bacteria; Pol III exhibits 3'-5'
CC exonuclease proofreading activity. The beta chain is required for
CC initiation of replication as well as for processivity of DNA
CC replication. {ECO:0000250|UniProtKB:P0A988}.
CC -!- SUBUNIT: Forms a ring-shaped head-to-tail homodimer (PubMed:25170813)
CC around DNA which binds and tethers DNA polymerases and other proteins
CC to the DNA (By similarity). The DNA replisome complex has a single
CC clamp-loading complex (3 tau and 1 each of delta, delta', psi and chi
CC subunits) which binds 3 Pol III cores (1 core on the leading strand and
CC 2 on the lagging strand) each with a beta sliding clamp dimer.
CC Additional proteins in the replisome are other copies of gamma, psi and
CC chi, Ssb, DNA helicase and RNA primase. {ECO:0000250|UniProtKB:P0A988,
CC ECO:0000269|PubMed:25170813}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P0A988}.
CC -!- SIMILARITY: Belongs to the beta sliding clamp family. {ECO:0000305}.
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DR EMBL; AE000516; AAK44225.1; -; Genomic_DNA.
DR PIR; F70850; F70850.
DR RefSeq; WP_003400271.1; NZ_KK341227.1.
DR PDB; 4TR7; X-ray; 2.29 A; A/B=1-402.
DR PDBsum; 4TR7; -.
DR AlphaFoldDB; P9WNU0; -.
DR SMR; P9WNU0; -.
DR EnsemblBacteria; AAK44225; AAK44225; MT0002.
DR KEGG; mtc:MT0002; -.
DR PATRIC; fig|83331.31.peg.2; -.
DR HOGENOM; CLU_038149_1_1_11; -.
DR Proteomes; UP000001020; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0009360; C:DNA polymerase III complex; IEA:InterPro.
DR GO; GO:0008408; F:3'-5' exonuclease activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR CDD; cd00140; beta_clamp; 1.
DR InterPro; IPR001001; DNA_polIII_beta.
DR InterPro; IPR022635; DNA_polIII_beta_C.
DR InterPro; IPR022637; DNA_polIII_beta_cen.
DR InterPro; IPR022634; DNA_polIII_beta_N.
DR PANTHER; PTHR30478; PTHR30478; 1.
DR Pfam; PF00712; DNA_pol3_beta; 1.
DR Pfam; PF02767; DNA_pol3_beta_2; 1.
DR Pfam; PF02768; DNA_pol3_beta_3; 1.
DR PIRSF; PIRSF000804; DNA_pol_III_b; 1.
DR SMART; SM00480; POL3Bc; 1.
DR TIGRFAMs; TIGR00663; dnan; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; DNA replication; DNA-binding;
KW DNA-directed DNA polymerase; Nucleotidyltransferase; Transferase.
FT CHAIN 1..402
FT /note="Beta sliding clamp"
FT /id="PRO_0000427068"
FT STRAND 14..18
FT /evidence="ECO:0007829|PDB:4TR7"
FT HELIX 19..30
FT /evidence="ECO:0007829|PDB:4TR7"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:4TR7"
FT STRAND 44..49
FT /evidence="ECO:0007829|PDB:4TR7"
FT STRAND 51..58
FT /evidence="ECO:0007829|PDB:4TR7"
FT STRAND 60..64
FT /evidence="ECO:0007829|PDB:4TR7"
FT STRAND 66..70
FT /evidence="ECO:0007829|PDB:4TR7"
FT STRAND 72..75
FT /evidence="ECO:0007829|PDB:4TR7"
FT STRAND 77..82
FT /evidence="ECO:0007829|PDB:4TR7"
FT HELIX 83..92
FT /evidence="ECO:0007829|PDB:4TR7"
FT STRAND 95..103
FT /evidence="ECO:0007829|PDB:4TR7"
FT STRAND 106..111
FT /evidence="ECO:0007829|PDB:4TR7"
FT STRAND 114..119
FT /evidence="ECO:0007829|PDB:4TR7"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:4TR7"
FT STRAND 135..139
FT /evidence="ECO:0007829|PDB:4TR7"
FT HELIX 141..152
FT /evidence="ECO:0007829|PDB:4TR7"
FT HELIX 162..164
FT /evidence="ECO:0007829|PDB:4TR7"
FT STRAND 165..172
FT /evidence="ECO:0007829|PDB:4TR7"
FT STRAND 175..181
FT /evidence="ECO:0007829|PDB:4TR7"
FT STRAND 183..192
FT /evidence="ECO:0007829|PDB:4TR7"
FT STRAND 201..207
FT /evidence="ECO:0007829|PDB:4TR7"
FT HELIX 208..216
FT /evidence="ECO:0007829|PDB:4TR7"
FT STRAND 224..227
FT /evidence="ECO:0007829|PDB:4TR7"
FT STRAND 239..244
FT /evidence="ECO:0007829|PDB:4TR7"
FT STRAND 247..252
FT /evidence="ECO:0007829|PDB:4TR7"
FT HELIX 262..264
FT /evidence="ECO:0007829|PDB:4TR7"
FT STRAND 267..276
FT /evidence="ECO:0007829|PDB:4TR7"
FT HELIX 277..288
FT /evidence="ECO:0007829|PDB:4TR7"
FT HELIX 292..294
FT /evidence="ECO:0007829|PDB:4TR7"
FT STRAND 297..302
FT /evidence="ECO:0007829|PDB:4TR7"
FT STRAND 305..312
FT /evidence="ECO:0007829|PDB:4TR7"
FT TURN 313..315
FT /evidence="ECO:0007829|PDB:4TR7"
FT STRAND 316..323
FT /evidence="ECO:0007829|PDB:4TR7"
FT STRAND 325..329
FT /evidence="ECO:0007829|PDB:4TR7"
FT STRAND 331..335
FT /evidence="ECO:0007829|PDB:4TR7"
FT HELIX 337..345
FT /evidence="ECO:0007829|PDB:4TR7"
FT STRAND 349..356
FT /evidence="ECO:0007829|PDB:4TR7"
FT STRAND 363..368
FT /evidence="ECO:0007829|PDB:4TR7"
FT STRAND 390..395
FT /evidence="ECO:0007829|PDB:4TR7"
SQ SEQUENCE 402 AA; 42113 MW; 1AB4B6D18653B42D CRC64;
MDAATTRVGL TDLTFRLLRE SFADAVSWVA KNLPARPAVP VLSGVLLTGS DNGLTISGFD
YEVSAEAQVG AEIVSPGSVL VSGRLLSDIT RALPNKPVDV HVEGNRVALT CGNARFSLPT
MPVEDYPTLP TLPEETGLLP AELFAEAISQ VAIAAGRDDT LPMLTGIRVE ILGETVVLAA
TDRFRLAVRE LKWSASSPDI EAAVLVPAKT LAEAAKAGIG GSDVRLSLGT GPGVGKDGLL
GISGNGKRST TRLLDAEFPK FRQLLPTEHT AVATMDVAEL IEAIKLVALV ADRGAQVRME
FADGSVRLSA GADDVGRAEE DLVVDYAGEP LTIAFNPTYL TDGLSSLRSE RVSFGFTTAG
KPALLRPVSG DDRPVAGLNG NGPFPAVSTD YVYLLMPVRL PG
